Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.

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Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme.Heme-dependent Inactivation of 5-Aminolevulinate Synthase from Caulobacter crescentus

P2860

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Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.

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2015 nî lūn-bûn

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2015年論文

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Human Erythroid 5-Aminolevulin ...... m and Enhance Product Release.

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Human Erythroid 5-Aminolevulin ...... m and Enhance Product Release.

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Human Erythroid 5-Aminolevulin ...... m and Enhance Product Release.

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Human Erythroid 5-Aminolevulin ...... m and Enhance Product Release.

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Human Erythroid 5-Aminolevulin ...... m and Enhance Product Release.

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Human Erythroid 5-Aminolevulin ...... m and Enhance Product Release.

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P1476

Human Erythroid 5-Aminolevulin ...... um and Enhance Product Release

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P2093

Erica J Fratz

http://www.w3.org/2001/XMLSchema#string

Gloria C Ferreira

http://www.w3.org/2001/XMLSchema#string

Gregory A Hunter

http://www.w3.org/2001/XMLSchema#string

Jean-Charles Deybach

http://www.w3.org/2001/XMLSchema#string

Jerome Clayton

http://www.w3.org/2001/XMLSchema#string

Sarah Ducamp

http://www.w3.org/2001/XMLSchema#string

Vladimir N Uversky

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P2860

Circular permutation of 5-aminolevulinate synthase. Mapping the polypeptide chain to its function

Erythropoietic protoporphyria

Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia

The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis

Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition

Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.

C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload

Measurement of protein using bicinchoninic acid

Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in pigeon. The enzymes incorporate the same alpha-subunit

Purification and structure of rat erythroid-specific delta-aminolevulinate synthase

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5617-5631

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scholarly article

P356

10.1021/ACS.BIOCHEM.5B00407

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English

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http://www.w3.org/2001/XMLSchema#string

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Laurent Gouya

Leonid Breydo

Hervé Puy

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2015-09-02T00:00:00Z

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26300302

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4573335

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Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.

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P2860

P2860

Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.

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P1433

P1476

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P2860

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P356

P407

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P1476

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P31

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P50

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P932